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Structural basis for detoxification and oxidative stress protection in membranes
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2006 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 360, no 5, 934-945 p.Article in journal (Refereed) Published
Abstract [en]

Synthesis of mediators of fever, pain and inflammation as well as protection against reactive molecules and oxidative stress is a hallmark of the MAPEG superfamily (membrane associated proteins in eicosanoid and glutathione metabolism). The structure of a MAPEG member, rat mictosomal glutathione transferase 1, at 3.2 angstrom resolution, solved here in complex with glutathione by electron crystallography, defines the active site location and a cytosolic domain involved in enzyme activation. The glutathione binding site is found to be different from that of the canonical soluble glutathione transferases. The architecture of the homotrimer supports a catalytic mechanism involving subunit interactions and reveals both cytosolic and membraneous substrate entry sites, providing a rationale for the membrane location of the enzyme.

Place, publisher, year, edition, pages
2006. Vol. 360, no 5, 934-945 p.
Keyword [en]
membrane protein, oxidative stress, enzymology, protein structure, electron crystallography, microsomal glutathione transferase, leukotriene c-4 synthase, 6 angstrom resolution, s-transferase, electron crystallography, purification, activation, substrate, superfamily, microscopy
Identifiers
URN: urn:nbn:se:kth:diva-15910DOI: 10.1016/j.jmb.2006.05.056ISI: 000239670200002OAI: oai:DiVA.org:kth-15910DiVA: diva2:333952
Note
QC 20100525Available from: 2010-08-05 Created: 2010-08-05 Last updated: 2017-12-12Bibliographically approved

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Hebert, Hans

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